Regulation of mixotrophy in <i>Synechocystis</i> by a rhomboid protease.

ABSTRACT: The intramembrane 'rhomboid' protease family is almost ubiquitous across evolution, with its well-conserved transmembrane domains typified in crystal structures of bacterial representatives, such as the Escherichia coli GlpG. In contrast with accumulating data on rhomboid function in higher organisms, where roles in human disease are an incentive for study, findings remain sparse about the functions and substrates of the prokaryotic enzymes, even though these provided the earliest protein structures. In particular, nothing at all is known about the rhomboid proteases of photosynthetic prokaryotes despite the importance of cyanobacteria as relatives of the progenitor of chloroplasts. Findings relating to the cyanobacterial enzymes would complement data on plant plastid rhomboids from

SUBMITTER: Ibrahim IM 

PROVIDER: S-EPMC12944812 | biostudies-literature | 2026 Feb

REPOSITORIES: biostudies-literature